V. Castillo

发表

The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case.

A. Espargaró, S. Ventura, N. S. de Groot, 2008, Journal of molecular biology.

AGGRESCAN: method, application, and perspectives for drug design.

Salvador Ventura, Virginia Castillo, Ricardo Graña-Montes, 2012, Methods in molecular biology.

The aggregation properties of Escherichia coli proteins associated with their cellular abundance.

Ricardo Graña-Montes, S. Ventura, V. Castillo, 2011, Biotechnology journal.

Trifluoroethanol Modulates Amyloid Formation by the All α-Helical URN1 FF Domain

S. Ventura, V. Castillo, P. Marinelli, 2013, International journal of molecular sciences.

Energy barriers for HET‐s prion forming domain amyloid formation

R. Sabaté, A. Espargaró, S. Ventura, 2009, The FEBS journal.

Amyloidogenic Regions and Interaction Surfaces Overlap in Globular Proteins Related to Conformational Diseases

Salvador Ventura, Virginia Castillo, S. Ventura, 2009, PLoS Comput. Biol..

Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown.

A. Goldberg, T. Akopian, A. Kisselev, 1999, Molecular cell.

Designing out disulfide bonds of leech carboxypeptidase inhibitor: implications for its folding, stability and function.

F. Avilés, S. Ventura, Sílvia Bronsoms, 2009, Journal of molecular biology.

The N-terminal Helix Controls the Transition between the Soluble and Amyloid States of an FF Domain

F. Chiti, S. Ventura, V. Castillo, 2013, PloS one.

Prediction of the aggregation propensity of proteins from the primary sequence: Aggregation properties of proteomes

Raimon Sabate, Salvador Ventura, Virginia Castillo, 2011, Biotechnology journal.

Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case.

A. Velázquez‐Campoy, J. Sancho, Ricardo Graña-Montes, 2012, Antioxidants & redox signaling.

Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria

A. Espargaró, S. Ventura, J. Vendrell, 2010, Proteomics.

The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case.

A. Espargaró, S. Ventura, N. S. de Groot, 2008, Journal of molecular biology.